Purification and some properties of glutathione S-transferase from Escherichia coli B.
Glutathione S-transferase was purified approximately 2,300-fold from cell extracts of Escherichia coli B with a 7.5% activity yield. The molecular weight of the enzyme was 45,000, and the enzyme appeared to consist of two homogeneous subunits. The enzyme was almost specific to 1-chloro-2,4-dinitrobe...
保存先:
| 出版年: | J Bacteriol |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1989
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC210469/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2553668/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.171.11.6039-6042.1989 |
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